ID C4L6Y5_EXISA Unreviewed; 372 AA.
AC C4L6Y5;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Peptidase T-like protein {ECO:0000313|EMBL:ACQ70078.1};
GN OrderedLocusNames=EAT1b_1150 {ECO:0000313|EMBL:ACQ70078.1};
OS Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=360911 {ECO:0000313|EMBL:ACQ70078.1, ECO:0000313|Proteomes:UP000000716};
RN [1] {ECO:0000313|EMBL:ACQ70078.1, ECO:0000313|Proteomes:UP000000716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1283 / AT1b {ECO:0000313|Proteomes:UP000000716};
RX PubMed=21460088; DOI=10.1128/JB.00303-11;
RA Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina Del Rio T.,
RA Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA Hendrix C., Richardson P., Tiedje J.M.;
RT "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT AT1b.";
RL J. Bacteriol. 193:2880-2881(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR001123-2};
CC -!- SIMILARITY: Belongs to the peptidase M42 family.
CC {ECO:0000256|PIRNR:PIRNR001123}.
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DR EMBL; CP001615; ACQ70078.1; -; Genomic_DNA.
DR RefSeq; WP_012727197.1; NC_012673.1.
DR AlphaFoldDB; C4L6Y5; -.
DR STRING; 360911.EAT1b_1150; -.
DR KEGG; eat:EAT1b_1150; -.
DR eggNOG; COG2195; Bacteria.
DR HOGENOM; CLU_021802_6_0_9; -.
DR OrthoDB; 9776600at2; -.
DR Proteomes; UP000000716; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR010162; PepT-like.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR008007; Peptidase_M42.
DR NCBIfam; TIGR01883; PepT-like; 1.
DR PANTHER; PTHR42994; PEPTIDASE T; 1.
DR PANTHER; PTHR42994:SF2; T, PUTATIVE-RELATED; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF001123; PepA_GA; 3.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 177..263
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 372 AA; 40049 MW; 49525263BDBECB6F CRC64;
MSSRVTETFM DLVRIDSESY AEGPFLDELK ERCARMGLEI DEDDSKDRTG LGSNNLIARL
KGDSSIEPLF LSAHIDTVSP GKGIVPIIRD DIVFSEGETI LAADDKAGIA IMLEVVERLQ
SEGARHGPIE LVFTPGEEVG LLGAKALDMS TIQATHGLIL DNGGSVGGII LSSPSMFSLQ
VDIHGRAAHA GLEPEKGISA LLIASDAIQN MKLGRISEKT TANIGKISGG TGSNVVMEQV
TLVGEARSLD HEACVDQVKH MILAFEQAAS NHGGTVDIKT EQMIRSYRFS EDEPFVQHVA
KALTDHSFEV RYEHSGGGSD ANVFNESGKV ALNVSIGYEA IHTIDESIPI KELEDSVSFV
LRVIETMQTF RS
//
